1HR8

Yeast Mitochondrial Processing Peptidase beta-E73Q Mutant Complexed with Cytochrome C Oxidase IV Signal Peptide

Summary for 1HR8

• Entry DOI: 10.2210/pdb1hr8/pdb
• Related: 1HR6 1HR7 1HR9
• Descriptor: MITOCHONDRIAL PROCESSING PEPTIDASE ALPHA SUBUNIT, MITOCHONDRIAL PROCESSING PEPTIDASE BETA SUBUNIT, CYTOCHROME C OXIDASE POLYPEPTIDE IV, ... (6 entities in total)
• Functional Keywords: hxxeh zinc-binding motif, hydrolase
• Biological source: Saccharomyces cerevisiae (baker's yeast); More
• Cellular location: Mitochondrion matrix: P11914 P10507; Mitochondrion inner membrane: P04037
• Total number of polymer chains: 12
• Total formula weight: 417893.63

Authors

Taylor, A.B.,Smith, B.S.,Kitada, S.,Kojima, K.,Miyaura, H.,Otwinowski, Z.,Ito, A.,Deisenhofer, J. (deposition date: 2000-12-21, release date: 2001-07-11, Last modification date: 2023-08-09)

Primary citation

Taylor, A.B.,Smith, B.S.,Kitada, S.,Kojima, K.,Miyaura, H.,Otwinowski, Z.,Ito, A.,Deisenhofer, J.
Crystal structures of mitochondrial processing peptidase reveal the mode for specific cleavage of import signal sequences.
Structure, 9:615-625, 2001

PubMed Abstract: Mitochondrial processing peptidase (MPP) is a metalloendopeptidase that cleaves the N-terminal signal sequences of nuclear-encoded proteins targeted for transport from the cytosol to the mitochondria. Mitochondrial signal sequences vary in length and sequence, but each is cleaved at a single specific site by MPP. The cleavage sites typically contain an arginine at position -2 (in the N-terminal portion) from the scissile peptide bond in addition to other distal basic residues, and an aromatic residue at position +1. Mitochondrial import machinery recognizes amphiphilic helical conformations in signal sequences. However, it is unclear how MPP specifically recognizes diverse presequence substrates.

PubMed: 11470436
DOI: 10.1016/S0969-2126(01)00621-9

Experimental method

X-RAY DIFFRACTION (2.7 Å)